Title: Human Physiology Dr. Phillip Stepp
1Human PhysiologyDr. Phillip Stepp
- Jan 20th, 2010
- 20 Trustee Science Center
- 1000-1100 AM M/W/F
2- Human Physiology (BIOL 206) Spring 2010
- Dr. Phillip Stepp
- Office 102 Trustee Science Center
- Email pstepp_at_drury.edu or pwsneuro_at_yahoo.com
- Text Human Physiology by Fox, 9th Edition
- Course Description This course is designed to
give students an in-depth understanding of the
various physiological systems in humans. Through
a combination of labs and lectures, students will
gain an appreciation for the manner in which the
body coordinates and executes physiological
functions. Students will also develop an
appreciation for the complexity of the human body
and the organization required for the proper
homeostatic balance the body must maintain in
order for life to continue. Throughout the
semester, students will consider anatomy,
physiology, and biochemistry, of the body and the
interaction of the various organ systems of the
human body.
3- Policies (read carefully)
- A. Students will be expected to be on-time for
each lecture and lab and to remain in class until
dismissed. Late arrivals and early departures
will need to be discussed since they tend to
disrupt the class. - B. Attendance is expected for all lectures and
labs. When absent, every student is responsible
for obtaining class notes and homework
assignments from other students in the class.
Therefore, you need to develop responsible
student contacts. By stating this in the
syllabus, you are now aware that no late homework
assignments will be accepted. If an assignment
is due and you know that you will not be in
class, have another student hand it in for you.
All absences will be recorded and any student
with three or more absences, for any reason, will
be reported to the Academic Dean and the
Registrars Office and strongly encouraged to
drop the course. - C. Exams may only be made up with prior
notification or if an emergency situation arises.
All make-up exams will be given at the end of
the semester.
4- D. All exams will be individual efforts without
notes or open books. All electronic devices
(computers, cell phones, calculators, etc.) will
be turned off and stored away (and out of sight).
Homework assignments need to be started early
enough in order to avoid waiting until the last
minute and handing in a poor quality assignment.
Homework assignments can be worked on together.
In fact, I encourage students to discuss the
information in the homework assignments to better
understand the material. HOWEVER, simply copying
any homework in attempt to complete it on-time
will be considered academic dishonesty. Also,
providing your homework so that another student
may simply copy your answers will also be
considered academic dishonesty. Any academic
dishonesty will be dealt with seriously involving
the notification of the Academic Dean. This
could result in course failure and/or dismissal
from the program. - E. IMPORTANT NOTE ALL FOOD AND DRINKS ARE
STRICTLY PROHIBITED FROM THE LAB ROOMS AT ALL
TIMES. THIS WILL BE STRICTLY ENFORCED. - F. All cell phones need to be turned off
during lectures and talking during lectures will
not be tolerated and students may be requested to
leave. An increasing number of complaints by
students over the past few semesters has prompted
this statement.
5- Grading System Final grades will be determined
as follows - Five lab assignments 30 pts. each 150 pts.
- Five lecture exams 100 pts. each 500 pts.
- Class Participation 50 pts.
- Total 700 pts.
-
- A 630 700 pts. (90) C 490 559 pts.
(70-79) - B 560 - 629 pts. (80-89)D 420 489 pts.
(60-69) - The quizzes and exams are designed to provide
students with an opportunity to think critically
and not simply to memorize information. Labs are
designed to provide hands-on experiences and to
promote collaborative learning.
6Human Physiology Tentative Schedule (Spring
2010) Week of Lecture/Lab 1/20 Intro
to Physiology (Ch 1, 2, 3) Chemical
Composition of the Body, Cellular Structure
1/25 Intro to Physiology II (Ch 4, 5,
6) Cellular Metabolism Interactions 2/1 C
h 7- Neurons and Synapses 2/8 Ch 8- The
Central Nervous System Crayfish Nerve Lesion
Lab 2/15 Ch 9- The Autonomic Nervous
System 2/22 Lecture Exam 1 Ch 10-
Sensory Physiology 3/1 Ch 12- Muscle
Mechanisms of Contraction and Neural
Control Sensory Physiology Lab 3/8 Ch 12-
Muscle Mechanisms of Contraction and Neural
Control Fatal Vision go-cart driving
PIZZA!!!! Lecture Exam 2
73/15 Ch 13- Heart and Circulation Human
ECG/Diving Response Lab 3/22 SPRING
BREAK!!! 3/29 Ch 14- Cardiac Output, Blood
Flow, and Blood Pressure Ch 15- Immune
System 4/5 Lecture Exam 3 Ch 16-
Respiratory Physiology 4/12 Ch 17- Physiology
of the Kidney Respiration Kidney
Lab 4/19 Ch 18- Digestive System 4/26 L
ecture Exam 4 Ch 11- Endocrine Glands
Secretion and Action of Hormones 5/3 Ch 19-
Regulation of Metabolism Goldfish Metabolism
Lab Ch 20- Reproduction Finals Week
(5/10) Lecture Exam 5
8Human Physiology Introduction- Part I
9Human Physiology
- Physiology the study of nature
- More specifically the study of how things
function - French physiologist Claude Bernard is the father
of modern physiology - Stated that the internal environment stays
relatively constant despite external conditions - Known as homeostasis- the maintainence of
internal physiological conditions
10Homeostatic Mechanisms
- Homeostasis maintained my neg feedback loops
- Body has a set point for many physiological
conditions - Integrating centers monitor information from
sensors, and make corrections and adjustments - Integrating centers act on effectors to increase
or decrease the activity of a particular system-
usually a muscle or gland - A Negative feedback loop is a system that
corrects for deviation from the set point by
moving the system in a negative (or reverse)
direction than the current conditions
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13Homeostatic Mechanisms
- Example- sweating/shivering
- Normal body temp is about 37 C
- If body temp increases ????
- If body temp decreases ????
- Some rare cases have positive feedback- action of
effectors amplifies the changes that stimulated
the effectors - Example- blood clotting
14Atoms, Ions Chemical Bonds
- Atom- smallest unit of chemical element
- Has protons (), neutrons in nucleus, electrons
(-) in orbitals - protonselectrons
- Molecules are formed by sharing of electrons-
form chemical bonds - of bonds determined by of electrons it takes
to complete outermost shell - Hydrogen can take one, carbon can take 4
15Covalent Bonds
- Covalent bonds formed when identical atoms share
valence electrons- electrons are equally shared
(ex- H2 or O2) - Since e- are equally shared, they are nonpolar
- Covalent bonds with different atoms are polar-
more e- might be pulled to one side of the
molecule than the other (ex- H20)
16Ionic Bonds
- Ionic bonds result when 1 valence e- from one
atom are transferred to a 2nd atom- no sharing - First atom loses e-, so it becomes charged ion
(anion) - Second atom gains e-, so it becomes negatively
charged ion (cation) - NaCl is an example- in water, dissociated into
Na and Cl-
17Ionic Bonds
- Ionic bonds are weaker than covalent polar bonds,
and dissociate easily in water - Na and Cl- attract H20 molecules, and the H20 in
turn attract other molecules, forming hydration
spheres around each ion - This is what makes a molecule soluable in
water - Hydrophilic molecules form hydration spheres
around themselves due to charge differences (ex
glucose) - Hydrophobic molecules have nonpolar covalent
bonds and do not form hydration spheres-
insoluble in water
18Hydrogen Bonds
- When H forms a polar covalent bond with O or N,
the H gains a charge due to the e- being toward
the other atom - Since H now has a slight charge, it has weak
attraction for another electronegative atom (O or
N) that is near it- this is a hydrogen bond - H bonds are weak, but important because they are
involved for folding and 3D shapes of large
organic molecules (proteins, DNA) - Also H bonds can form between H20 molecules-
important in creating surface tension in water
and lungs
19Acids, Bases, and pH Scale
- Some water molecules ionize to form H (proton)
and OH- (hydroxyl ion) - Solution with 10-7 molar concentration of H and
OH- is considered neutral (pH 7) - Solution with higher H is acidic- can release
H protons into solution (pH 0-7) - Solution with lower H is basic- it removes H
from solution (pH 7-14)
20Carbohydrates
- Carbohydrates contain contain carbon, hydrogen,
and oxygen in a certain proportion - CnH2nOn
- Monosaccharide- simple sugars
- C6H12O6 can be for Glucose, Galactose, or
Fructose, depending on atom arrangement - Disaccharide- two mono- joined by covalent bond
to make a double sugar (ex sucrose) - Polysaccharide- numerous mono- joined together
(ex glycogen)
21Lipids
- Have varying chemical structure, but are all
insoluble in water - Because they are mostly hydrocarbon chains and
rings which are nonpolar and hydrophobic - Triglycerides- includes fat and oil, formed by
condensation of one glycerol with three fatty
acids - Saturated- C in chain are joined by single
covalent bond so each C can also be bound to 2 H
atoms - Unsaturated- C in chain are joined by some double
covalent bonds, and not all C have 2 H - Steroids are also considered lipids- derived from
cholesterol, and important for production of sex
steroids (estrogen, progesterone, testosterone)
and corticosteroids (hydrocortisone and
aldosterone)
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23Formation of Triglycerides
24Lipids- Phospholipids
- Lipid molecules that contain a phosphate group
- Have a polar end (phosphate group) that is
hydrophilic - Have a nonpolar end (fatty acid molecules) that
are hydrophobic - In water, plipids form micelles- hollow bubbles
of plipds with hydrophilic heads towards H20, and
tails away from H20 - Very important in forming the cell membrane, as
well as decreasing H20 surface tension
25Phospholipid Structure
26Proteins
- Proteins are composed of amino acids (AA)-
compound with an amino group (NH2) on one end,
and a carboxyl group (COOH) on the other - There are 20 different amino acids
- AA can be joined together by peptide bonds to
form peptides or polypeptides - If 100 AA are linked, the product is a protein
27Proteins
- Proteins have
- Primary structure- sequence of AA in protein
- Secondary Structure- shape of the protein due to
H bonds - Either alpha helix or beta sheet
- Tertiary structure- how the protein bends and
folds on itself due to interactions among AAs - Can denature proteins by various means, including
pH, and heat - Quaternary structure- how a number of polypeptide
chains are bound together
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31Cell Structure and Cytology
- Human body is composed of 60 trillion to 100
trillion cells (only 270 to 300 individual
different types) - Cells- most basic, independent unit of life (part
of the Cell Theory) - Metabolism - sum total of all reactions that
occur with the body - catabolic reactions (chemical breakdown) vs.
anabolic reactions (chemical build-up) - Cellular Diversity (270 to 300 individual
different types) - size range - few micrometers (µm) to approx. 140
µm (example an RBC is approx. 7.5um in diameter) - function and structure are closely related
(important point to remember throughout this
course)
32- Chemistry of the cell important elements
- carbon, oxygen, hydrogen, nitrogen, phosphorus,
sulfur, calcium, potassium, sodium, and magnesium
( most common in the body at approximately 65) - In fact Oxygen (65), Carbon (18), Hydrogen
(10) and Nitrogen (3) - Water (universal solvent with several other
properties) and dissolved substances (solute) - electrolytes compounds that ionize in water
an carry an electrical charge (acids, bases and
salts) - 4 major types of macromolecules proteins,
carbohydrates, lipids, and nucleic acids with
building blocks of amino acids, monosaccharides,
fatty acids and glycerol and nucleotides,
respectively.
33Plasma Membrane
- cell (plasma) membrane - 6.5 to 10 nm (65 to 100
A) thick - phospholipid bilayer (with some cholesterol
molecules in hydrophobic region) - hydrophilic (phosphate heads) vs. hydrophobic
(fatty acid tails) portions of phospholipids - scattered membrane proteins (peripheral or
surface and integral or embedded) - may possess pores (0.7 to 1.0 nm or 7 to 10 A)
for movement through the membrane - may be glycosylated, even to point where it forms
a sugar coating called a glycocalyx - semipermeable barrier - selective exchange of
materials across the membrane - passive and
active processes (see notes below)
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35Plasma Membrane
- The six major factors that affect membrane
transport - membrane structure the phosholipid bilayer and
scattered proteins - size of molecules smaller molecules pass
through with ease - ionic charge charged molecules do not pass
through easily - lipid solubility steroids and other lipids pass
through with ease - carrier molecules the number of embedded
proteins with pores makes a difference - pressure differences greater pressures help
push substances through the membrane
36Plasma Membrane
- Passive (does not use cellular (ATP) energy
- Simple diffusion
- Facilitated diffusion
- Osmosis
- Filtration
- Dialysis (artificial)
- Active (uses ATP (cellular) energy
- Active transport (uses carrier molecules)
- Exocytosis (secretion)
- Endocytosis (uptake and vesicle formation)
- Pinocytosis (uptake of liquids)
- Phagocytosis (uptake of solids)
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39Cytoplasm
- Cytoplasm - gel-like substance (colloidal
suspension) that fills the cell's interior of a
cell that is - 80-90 water, filled with metabolites, waste
materials, building blocks, enzymes, etc. - suspends the variety of organelles and inorganic
colloids - Very important dynamic substance where many
metabolic chemical reactions take place
40Cellular Organelles
- Organelles - variety of distinct cellular
components - some membranous (RER, SER, Golgi complex, etc.)
- some vesicular or granular (lysosomes,
peroxisomes, melanin, glycogen, etc.) - some filamentous (microtubules, intermediate
filaments, microfilaments, etc.)
41Endoplasmic Reticulum
- Endoplasmic reticulum - 2 types (rough ER vs.
smooth ER) - membranous sacs or tubules with their interior
regions referred to as the cisternae - may attach to the inside of the cell membrane and
possibly to the nucleus or other organelles - Rough ER (RER) - with ribosomes attached for
protein synthesis, primarily secretory proteins
(pinch off as vesicles) also, RER possesses
enzymes in the membranous walls that produce some
lipids - Smooth ER (SER) - lacks ribosomes also possesses
enzymes in its walls for lipid synthesis, but
unlike RER, most of the lipids are steroids also
contains enzymes that detoxify poisons (alcohol,
drugs, etc.)
42Ribosomes
- Ribosomes - small particles (12-15 nm in
diameter) required for protein synthesis each
ribosome consists of - Two subunits (60S and 40S), each composed of
protein and r-RNA. - May attach to membranes (primarily used to
produce secretory proteins) or may form
free-floating structures called polysomes or
polyribosomes (primarily used to produce
intracellular proteins).
43Golgi Complex
- Golgi complex - series of slightly curved,
flattened membranous sacs with vesicles located
near its expanded ends - Found near the nucleus and is continuous with the
(R)ER. - Packages secretory granules and plays a role in
lysosome formation. - Glycosylates proteins (adds CHOs) to form
glycoproteins and concentrates proteins (by
removing water) in mature secretory granules.
44Mitochondria
- Mitochondria - double-membraned organelle, found
to exist in various shapes and numbers. - The outer membrane is smooth whereas the inner
membrane is folded to form shelf-like cristae
to increase the membranes surface area. - The semisolid substance within the mitochondria
is called the matrix and is found between
cristae with ribosomes (w/ 50S and 30S subunits),
granules that bind to divalent cations (e.g.
Ca, Mg), and prokaryotic-like DNA and can
therefore self-duplicate to meet increased energy
demands. - They are often referred to as the powerhouse of
the cell because produces ATP - required for
metabolic energy. Their presence supports the
endosymbiotic theory (in plants, chloroplasts do
too).
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46Lysosomes Perixisomes
- Lysosomes - membrane-bound structure that possess
powerful digestive enzymes that appear granular
when inactive and vesicular when activeEnzymes
are capable of digesting proteins, lipids,
certain carbohydrates, DNA and RNA - When attached to phagocytic vesicles, lysosomes
are known as secondary lysosomes - digest to
provide cell with raw materials for synthetic
reactions in the cell - Remaining undigested materials in vacuoles -
residual body - May digest parts of the cell they reside in by
attaching to a vacuole or an intracellular
component - this is known as autophagocytosis - Peroxisomes - also known as microbodies and
resemble lysosomes - Possess powerful oxidative enzymes used to obtain
energy from molecules and enzymes that degrade
H2O2 into H2O and O2 (H2O2 is very toxic to the
cell) using an enzyme called catalase or
peroxidase.
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48Fibrils and Microtubules
- Fibrils and Microtubules - found coursing
throughout the cytoplasm making up the
"cytoskeleton". - Fibrils, also called microfilaments (6 nm), are
solid, rod-like structures that may occur in
bundles. They are composed of proteins,
especially actin and myosin. - Microtubules (25 nm) are hollow, tubular rods of
various lengths and are composed of protein
subunits called tubulin. - Microfilaments play a major role in muscle
contraction. - Microtubules direct intracellular movement,
especially the movement of secretory granules, by
using "MAPS" (microtubule associated proteins) -
like a conveyer belt. - A variety of intermediate filaments (10 nm) also
contribute to the cytoskeleton and cellular
connections.
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50Cilia and Flagella
- Cilia and flagella - basically, the same thing ?
cytoplasmic extensions of the cell with a core of
microtubules in the classic "9 2" arrangement. - The major difference, cilia are short and
numerous, and flagella are long and few in number
(usually one). - Cilia move substances along a cell surface,
whereas flagella typically move a cell. - At the base of each cilium or flagellum, is a
basal body composed of 9 triplets of
microtubules. They act as movement coordinators
for each cellular projection.
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52Centrosome and Centrioles
- Centrosome and Centrioles - the centrosome is a
spherical, non-membranous mass near the nucleus
that contains the paired, rod-shaped centrioles.
- Centrioles are composed of 27 microtubules
arranged in a pinwheel fashion with 9 sets of
triplets. The pair of centrioles are oriented at
right angles to each other and play a role in
mitosis and meiosis (cell division) by directing
the movement of chromosomes. - Cells that do not divide (mature muscle and nerve
cells) lack a centrosome.
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54Nucleus, Necleolus, and Chromatin
- Nucleus - large spherical structure encased by a
double membrane pores (approx. 40 to 45 nm thick)
called the nuclear envelope with many nuclear
pores (up to 25 of envelope surface. - The space in the membrane is called the
perinuclear cisterna (or space). - Two important structures within the nucleus are
the nucleolus and chromatin. They are found
embedded in the nucleoplasm. - Nucleolus - small nonmenbranous mass composed of
protein and RNA - Functions to produce ribosomal subunits which
leave the nucleus through nuclear pores to
function in the cytoplasm. - Chromatin - coiled, thread-like genetic material
composed of protein and DNA which functions to
control synthetic activity of the cell via
protein (enzyme) synthesis
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56Cell Division- Mitosis and Meiosis
- Mitosis - cell division where DNA replicates,
then divides once - most common type of all
division - Meiosis - cell division where DNA replicates,
then divides twice - only occurs in the testes
and ovaries
57DNA
- DNA - deoxyribonucleic acid composed of
nucleotides. - Each nucleotide has 3 parts phosphate, sugar,
and nitrogenous base. - Only the bases differ with 4 different types
adenine, guanine, cytosine, thymine. - Complementary base pairing A T and G C.
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60RNA
- RNA - composed of nucleotides, like DNA, except
no thymine. Instead RNA has uracil so A - U
pairs up - mRNA - carries the genetic message or "codon" (3
nucleotides long) produced from a DNA "triplet
therefore, has a complementary sequence. - There are 64 possible codon sequences coding for
only 20 different amino acids you will only
need to learn four specific codons. - tRNA - recognizes mRNA codon using a
complementary "anticodon" and delivers a specific
amino acid to a growing polypeptide chain. - rRNA - complexes with proteins to form ribosomes,
upon which proteins are produced - important codons AUG start codon and UAA,
UAG, and UGA stop codons - example sequence CCG GGA AUG CCU AGU GUG CAG UUG
UAA GCU RNA for 6 amino acids (start)
(stop)
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62Replication, Transcription and Translation
- Replication DNA makes exact (or nearly exact)
copy of itself - Transcription DNA makes RNA (makes all 3 types
ribosomal RNA, transfer RNA, and messenger RNA) - Translation protein synthesis (uses all 3 types
of RNA) and occurs on ribosomes (free or
membrane-bound)
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